title: Interfacial instability and DNA fork reversal by repair proteins.
abstract: A repair protein like RecG moves the stalled replication fork in the direction from the zipped to the unzipped state of DNA. It is proposed here that a softening of the zipped-unzipped interface at the fork results in the front propagating towards the unzipped side. In this scenario, an ordinary helicase destabilizes the zipped state locally near the interface and the fork propagates towards the zipped side. The softening of the interface can be produced by the aromatic interaction, predicted from the crystal structure, between RecG and the nascent broken base pairs at the Y-fork. A numerical analysis of the model also reveals the possibility of a stop and go type motion.
authors.affiliation: Institute of Physics, Bhubaneswar 751005, India. somen@iopb.res.in
authors.forename: Somendra M
authors.initials: SM
authors.lastname: Bhattacharjee
mesh_terms: D000465:Algorithms; D001703:Biophysics / Q000379:methods; D003460:Crystallization; D004247:DNA / Q000737:chemistry*; D004260:DNA Repair; D004261:DNA Replication; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry*; D015233:Models, Statistical; D008962:Models, Theoretical; D009690:Nucleic Acid Conformation; D013997:Time Factors
chemical_list: D029968:Escherichia coli Proteins; C071446:RecG protein, E coli; D004247:DNA